Proteolytic Enzymes
Proteolytic enzymes of pancreas.
Answer:
Proteolytic enzymes:
1. Trypsinogen:
- It is a single long polypeptide chain with molecular weight of 25,000
- It contains 229 amino acids
- It is converted into active trypsin by enterokinase.
Trypsinogen Actions:
- It converts proteins into proteoses and polypeptides by hydrolysis.
- Curdles milk.
- Accelerates blood clotting.
- Activates other enzymes of pancreas.
- It has autocatalytic action.
“Understanding proteolytic enzymes through FAQs: Composition, functions, and uses explained”
2. Chymotrypsinogen:
- It is a polypeptide with a molecular weight of 25,700.
- It has 246 amino acids.
- It is activated by trypsin.
Chymotrypsinogen Actions:
- Digests protein to small polypeptides.
- Causes more rapid digestion of milk.
3. Carboxypeptidases:
- They are activated by trypsin.
Carboxypeptidases Actions:
- They break the terminal bond of protein.
- Carboxypeptidase A splits the proteins into amino acids having aromatic side chains.
- Carboxypeptiase B splits the proteins into amino acids having basic side chains.
“Importance of studying proteolytic enzymes for biochemistry students: Questions explained”
4. Nucleases:
- They split nucleic acids into mononucleotides.
5. Proelastase:
- Proelastase is activated by trypsin.
Proelastase Actions:
- Causes digestion of elastin and other polypeptides.
“Factors influencing success with proteolytic enzyme studies: Q&A”
6. Collagenase:
- It is also activated by trypsin.
- It digests collagen.
- All these enzymes are secreted in inactive state.
- The inactive granules are activated in the duodenum where they act on proteins.
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